The Experts below are selected from a list of 2730 Experts worldwide ranked by ideXlab platform
Rotimi E Aluko - One of the best experts on this subject based on the ideXlab platform.
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Kinetics and molecular docKing studies of the Inhibitions of angiotensin converting enzyme and renin activities by hemp seed cannabis sativa l peptides
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Abraham T Girgih, Rong He, Rotimi E AlukoAbstract:Four novel peptide sequences (WVYY, WYT, SVYT, and IPAGV) identified from an enzymatic digest of hemp seed proteins were used for enzyme Inhibition Kinetics and molecular docKing studies. Results showed that WVYY (IC50 = 0.027 mM) was a more potent (p < 0.05) ACE-inhibitory peptide than WYT (IC50 = 0.574 mM). However, WYT (IC50 = 0.054 mM) and SVYT (IC50 = 0.063 mM) had similar renin-inhibitory activity, which was significantly better than that of IPAGV (IC50 = 0.093 mM). Kinetics studies showed that WVYY had a lower Inhibition Constant (Ki) of 0.06 mM and hence greater affinity for ACE when compared to the 1.83 mM obtained for WYT. SVYT had lowest Ki value of 0.89 mM against renin, when compared to the values obtained for WYT and IPAGV. Molecular docKing results showed that the higher inhibitory activities of WVYY and SVYT were due to the greater degree of noncovalent bond-based interactions with the enzyme protein, especially formation of higher numbers of hydrogen bonds with active site residues.
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Kinetics and molecular docKing studies of the Inhibitions of angiotensin converting enzyme and renin activities by hemp seed cannabis sativa l peptides
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Abraham T Girgih, Rotimi E AlukoAbstract:Four novel peptide sequences (WVYY, WYT, SVYT, and IPAGV) identified from an enzymatic digest of hemp seed proteins were used for enzyme Inhibition Kinetics and molecular docKing studies. Results showed that WVYY (IC50 = 0.027 mM) was a more potent (p < 0.05) ACE-inhibitory peptide than WYT (IC50 = 0.574 mM). However, WYT (IC50 = 0.054 mM) and SVYT (IC50 = 0.063 mM) had similar renin-inhibitory activity, which was significantly better than that of IPAGV (IC50 = 0.093 mM). Kinetics studies showed that WVYY had a lower Inhibition Constant (Ki) of 0.06 mM and hence greater affinity for ACE when compared to the 1.83 mM obtained for WYT. SVYT had lowest Ki value of 0.89 mM against renin, when compared to the values obtained for WYT and IPAGV. Molecular docKing results showed that the higher inhibitory activities of WVYY and SVYT were due to the greater degree of noncovalent bond-based interactions with the enzyme protein, especially formation of higher numbers of hydrogen bonds with active site residues.
Pyojam Park - One of the best experts on this subject based on the ideXlab platform.
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antihypertensive activity of chitin derivatives
Biopolymers, 2006Co-Authors: Jaeyoung Je, Pyojam ParkAbstract:To develop angiotensin I converting enzyme (ACE) inhibitory chitin derivatives based on the properties of ACE inhibitors, chitins with different degree of deacetylation were chemically modified by grafting 2-chloroethylamino hydrochloride onto chitin at the C-6 position. Three Kinds of chitin derivatives were prepared and designated as aminoethyl-chitin (AEC) with 10% degree of deacetylation, aminoethyl-chitin with 50% degree of deacetylation (AEC50), and aminoethyl-chitin with 90% degree of deacetylation (AEC90). IC50 values of three chitin derivatives on ACE were 0.064 μM (AEC), 0.038 μM (AEC50), and 0.103 μM (AEC90). The results of Dixon plots revealed that AEC50 was a competitive inhibitor, and the Inhibition Constant (Ki) value was 0.021 μM. In addition, the antihypertensive effect of AEC50 on spontaneously hypertensive rats (SHR) was evaluated, and the result showed that it effectively decreased systolic blood pressure (SBP) in a dose-dependent manner. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 250–254, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
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antihypertensive activity of chitin derivatives
Biopolymers, 2006Co-Authors: Jaeyoung Je, Pyojam ParkAbstract:To develop angiotensin I converting enzyme (ACE) inhibitory chitin derivatives based on the properties of ACE inhibitors, chitins with different degree of deacetylation were chemically modified by grafting 2-chloroethylamino hydrochloride onto chitin at the C-6 position. Three Kinds of chitin derivatives were prepared and designated as aminoethyl-chitin (AEC) with 10% degree of deacetylation, aminoethyl-chitin with 50% degree of deacetylation (AEC50), and aminoethyl-chitin with 90% degree of deacetylation (AEC90). IC50 values of three chitin derivatives on ACE were 0.064 μM (AEC), 0.038 μM (AEC50), and 0.103 μM (AEC90). The results of Dixon plots revealed that AEC50 was a competitive inhibitor, and the Inhibition Constant (Ki) value was 0.021 μM. In addition, the antihypertensive effect of AEC50 on spontaneously hypertensive rats (SHR) was evaluated, and the result showed that it effectively decreased systolic blood pressure (SBP) in a dose-dependent manner. © 2006 Wiley Periodicals, Inc. Biopolymers 83: 250–254, 2006 This article was originally published online as an accepted preprint. The “Published Online” date corresponds to the preprint version. You can request a copy of the preprint by emailing the Biopolymers editorial office at biopolymers@wiley.com
Shahreen Kasim - One of the best experts on this subject based on the ideXlab platform.
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molecular docKing analysis of 6 paradol zingerone and zerumbone against human estrogen receptor alpha erɑ
International Journal of Integrated Engineering, 2018Co-Authors: Faez Sharif, Athirah Azirudin, Rd Rohmat Saedudin, Afdzal Mohd Yunus, Azzmer Azzar Abdul Hamid, Shahreen KasimAbstract:Molecular docKing was done to assess the binding affinity of 6-paradol (6PRD), Zingerone (ZGR) and Zerumbone (ZRB) ligand-ERα complex in comparison to Hydroxytamoxifen (HTMX). DocKing results showed that Glu353 and Arg394 active residues forms hydrogen bonding with 6PRD and ZGR. Glu353, Leu387 and Arg394 were the three identical residues found to formed hydrophobic interaction in HTMX-ERα, 6PRD-ERα and ZGR-ERα. HTMX showed lowest binding energy (-10.71 ± 0.43 kcal/mol) followed by ZRB (-8.66 ± 0.04 kcal/mol), 6PRD (-6.92 ± 0.14 kcal/mol) and ZGR (-5.93 ± 0.31 kcal/mol). Inhibition Constant (Ki) range of 6PRD-ERα was found to be drastically lower than HTMX-ERα, ZGR-ERα and ZRB-ERα. Based on the docKing analysis, the three bioactive compounds were showed to poses low potential as substitute towards tamoxifen. Future study is recommended for analysing 6PRD potential in substituting estradiol as Hormone Replacement Therapy (HRT) for breast cancer.
Abraham T Girgih - One of the best experts on this subject based on the ideXlab platform.
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Kinetics and molecular docKing studies of the Inhibitions of angiotensin converting enzyme and renin activities by hemp seed cannabis sativa l peptides
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Abraham T Girgih, Rong He, Rotimi E AlukoAbstract:Four novel peptide sequences (WVYY, WYT, SVYT, and IPAGV) identified from an enzymatic digest of hemp seed proteins were used for enzyme Inhibition Kinetics and molecular docKing studies. Results showed that WVYY (IC50 = 0.027 mM) was a more potent (p < 0.05) ACE-inhibitory peptide than WYT (IC50 = 0.574 mM). However, WYT (IC50 = 0.054 mM) and SVYT (IC50 = 0.063 mM) had similar renin-inhibitory activity, which was significantly better than that of IPAGV (IC50 = 0.093 mM). Kinetics studies showed that WVYY had a lower Inhibition Constant (Ki) of 0.06 mM and hence greater affinity for ACE when compared to the 1.83 mM obtained for WYT. SVYT had lowest Ki value of 0.89 mM against renin, when compared to the values obtained for WYT and IPAGV. Molecular docKing results showed that the higher inhibitory activities of WVYY and SVYT were due to the greater degree of noncovalent bond-based interactions with the enzyme protein, especially formation of higher numbers of hydrogen bonds with active site residues.
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Kinetics and molecular docKing studies of the Inhibitions of angiotensin converting enzyme and renin activities by hemp seed cannabis sativa l peptides
Journal of Agricultural and Food Chemistry, 2014Co-Authors: Abraham T Girgih, Rotimi E AlukoAbstract:Four novel peptide sequences (WVYY, WYT, SVYT, and IPAGV) identified from an enzymatic digest of hemp seed proteins were used for enzyme Inhibition Kinetics and molecular docKing studies. Results showed that WVYY (IC50 = 0.027 mM) was a more potent (p < 0.05) ACE-inhibitory peptide than WYT (IC50 = 0.574 mM). However, WYT (IC50 = 0.054 mM) and SVYT (IC50 = 0.063 mM) had similar renin-inhibitory activity, which was significantly better than that of IPAGV (IC50 = 0.093 mM). Kinetics studies showed that WVYY had a lower Inhibition Constant (Ki) of 0.06 mM and hence greater affinity for ACE when compared to the 1.83 mM obtained for WYT. SVYT had lowest Ki value of 0.89 mM against renin, when compared to the values obtained for WYT and IPAGV. Molecular docKing results showed that the higher inhibitory activities of WVYY and SVYT were due to the greater degree of noncovalent bond-based interactions with the enzyme protein, especially formation of higher numbers of hydrogen bonds with active site residues.
Lisa Dalla Via - One of the best experts on this subject based on the ideXlab platform.
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2 phenyloxazole 4 carboxamide as a scaffold for selective Inhibition of human monoamine oxidase b
ChemMedChem, 2019Co-Authors: Maria Luisa Di Paolo, Michael S Christodoulou, Alessandra M Calogero, Luca Pinzi, Giulio Rastelli, Daniele Passarella, Graziella Cappelletti, Lisa Dalla ViaAbstract:A series of 2-phenyloxazoles bearing an amide group at position 4 were designed and synthesized for evaluation as potential inhibitors of human recombinant monoamine oxidases (hrMAOs). Results of Kinetics experiments demonstrated that all compounds behave as competitive MAO inhibitors, with good selectivity toward the MAO-B isoform. The most potent and selective derivatives are characterized by Inhibition Constant (Ki ) values in the sub-micromolar range and a good selectivity index (Ki MAO-A /Ki MAO-B >50). Some derivatives were also found to be able to inhibit MAO activity in nerve growth factor (NGF)-differentiated PC12 cells, taken as a model of neuronal cells. In particular, 2-(2-hydroxyphenyl)-N-phenyloxazole-4-carboxamide (compound 4 a) may be a promising new scaffold, exerting the highest selectivity and inhibitory effect toward MAOs in NGF-differentiated PC12 cell lysates, without compromising cell viability. Molecular docKing analysis allowed a rationalization of the experimentally observed binding affinity and selectivity.